Details of SAPdb entry with Sequence LG |
Primary information | |
---|---|
SAPdb ID | 1282, |
PMID | 20307067 |
Peptide Name | Fmoc-Leu-Gly-OH |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | TEM (Transmission Electron Microscopy), SEM (Scanning Electron Microscopy) |
Solvent | NaCl solution containing hydroquinone |
Method | A stock solution of 0.24 mol dm-3 of dipeptide derivative in DMSO was prepared. Then 10 μL of the stock was added to 1 cm-3 of a solution containing 0.066 mol dm-3 hydroquinone and 0.1 mol dm-1 NaCl. Then 4 μL of 1 mol dm-3 NaOH was added to fully dissolve the dipeptide and 8 μL of 1 mol dm-3 HCl to bring pH 7. The final solution was introduced to the surface of the gold slide via an electrochemical flow cell. |
Conc | 1mg/ml |
Temperature | |
Incubation Time | 2 hours |
Year | 2010 |
Self assembly | Yes |
Type of Self assembly | Hydogel Membranes |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
Stable under acidic conditions on applying current | |
Hydrogel | |
NA | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1286, |
PMID | 22890605 |
Peptide Name | FmocLG |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Conjugate |
Conjugate partner | Fmoc(fluorenylmethoxycarbonyl) |
Technique | SEM (Scanning Electron Microscopy) |
Solvent | Sodium hydoxide(0.1 M ) |
Method | A 0.5 wt% stock solution of dipeptide at pH 9 – 10 prepaed by adding 1 equivalent of sodium hydroxide solution 0.1 M solution) with stirring to dissolve, 0.1 M HCl added to lower the pH of solution o 5. To form gels, 2 mL of stock solution was placed in a 7 mL Sterilin cup and UV light was irradiated from a 40 W Spectroline X-series UV lamp (wavelength 254 nm) . |
Conc | 5mg/ml |
Temperature | 5 |
Temperature | Room temperature |
Incubation Time | 14 hours |
Year | 2012 |
Self assembly | Yes |
Type of Self assembly | Opaque gel (Nanofibers) |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Hydrogel | |
70 | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1444, |
PMID | 24085660 |
Peptide Name | Fmoc-LG |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | TEM (Transmission Electron Microscopy) and WAXS(Wide Angle X - Ray scattering) |
Solvent | Water + 0.1M Hcl + 0.5 M NaOH |
Method | Fmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation. |
Conc | 10mmol/L |
Temperature | pH 10.5 |
Temperature | 4 °C |
Incubation Time | ~ 12 hours |
Year | 2013 |
Self assembly | No |
Type of Self assembly | No hydogel formation |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
None | |
NA | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1445, |
PMID | 24085660 |
Peptide Name | Fmoc-LG |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | TEM (Transmission Electron Microscopy) and WAXS(Wide Angle X - Ray scattering) |
Solvent | Water + 0.1M Hcl + 0.5 M NaOH |
Method | Fmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation. |
Conc | 10mmol/L |
Temperature | pH 7.6 |
Temperature | 4 °C |
Incubation Time | ~ 12 hours |
Year | 2013 |
Self assembly | Yes |
Type of Self assembly | Nanoribbon |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanoribbon | |
24 | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1446, |
PMID | 24085660 |
Peptide Name | Fmoc-LG |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | TEM (Transmission Electron Microscopy) and WAXS(Wide Angle X - Ray scattering) |
Solvent | Water + 0.1M Hcl + 0.5 M NaOH |
Method | Fmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation. |
Conc | 10mmol/L |
Temperature | pH 4.3 - 5.6 |
Temperature | 4 °C |
Incubation Time | ~ 12 hours |
Year | 2013 |
Self assembly | Yes |
Type of Self assembly | Twisted Ribbon |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanoribbon | |
13.5 | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1477, |
PMID | 22651803 |
Peptide Name | Dipeptide4 |
Peptide sequence | LG |
N-Terminal Modification | Napthalene |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | SEM (Scanning Electron Microscopy) and X - Ray Diffraction |
Solvent | Water + 0.1 M NaOH |
Method | 25mg of dipeptide was suspended in deionized 5ml water . An equimolar amount of NaOH (0.1 M,aq) was added, and the solution was gently stirred until a clear solution was formed. Glucono-δ- lactone (GdL) was added to the solution and the samples were gently swirled to dissolve the GdL before being left to stand for 24 h without stirring to form gel. |
Conc | 5mg/ml or 0.5%wt |
Temperature | Room temperature |
Incubation Time | 24 hours |
Year | 2012 |
Self assembly | Yes |
Type of Self assembly | Transparent or clear gel |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Hydrogel | |
NA | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1483, |
PMID | 22651803 |
Peptide Name | Dipeptide13 |
Peptide sequence | LG |
N-Terminal Modification | Napthalene |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Technique | SEM (Scanning Electron Microscopy) and X - Ray Diffraction |
Solvent | Water + 0.1 M NaOH |
Method | 25mg of dipeptide was suspended in deionized 5ml water . An equimolar amount of NaOH (0.1 M,aq) was added, and the solution was gently stirred until a clear solution was formed. Glucono-δ- lactone (GdL) was added to the solution and the samples were gently swirled to dissolve the GdL before being left to stand for 24 h without stirring to form gel. |
Conc | 5mg/ml or 0.5%wt |
Temperature | Room temperature |
Incubation Time | 24 hours |
Year | 2012 |
Self assembly | Yes |
Type of Self assembly | Transparent or clear gel |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Hydrogel | |
NA | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1507, |
PMID | 20307067 |
Peptide Name | Fmoc-Leu-Gly-OH |
Peptide sequence | LG |
N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | TEM (Transmission Electron Microscopy), SEM (Scanning Electron Microscopy) and SPR (Surface plasmon Resonance) spectroscopy |
Solvent | DMSO + hydroquinone + NaOH + HCl |
Method | Stock solution of 0.24 mol/L of peptide in DMSO prepared and 10 μl of this added to 1ml of 0.066 mol dm-3 of hydroquinone and 0.1 mol dm-1 NaCl + 8 μL of 1 mol dm-3 HCl to bring pH 7. The final solution was introduced to the surface of GOLD slide via an electrochemical cell. |
Conc | 1mg/ml |
Temperature | 7 |
Year | 2010 |
Self assembly | Yes |
Type of Self assembly | Thick layer of Hydrogel |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
Stable | |
Hydrogel | |
1000000 | |
LG | |
N.A. | |
Primary information | |
SAPdb ID | 1557, |
PMID | 21833387 |
Peptide Name | Peptide 2 |
Peptide sequence | LG |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 2 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | FE - SEM (Field Emission Scanning Electron Microscopy), TEM (Transmission Electron Microscopy) and AFM (Atomic Force Microscopy) |
Solvent | Water |
Method | Each of these peptides (0.06 mmol) was dissolved in 1mLwater of pH 6.96 and allowed to age for 24 h |
Conc | 0.06mmol |
Temperature | 6.96 |
Temperature | 37°C |
Incubation Time | 24 - 48 hours |
Year | 2011 |
Self assembly | Yes |
Type of Self assembly | Spherical structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
Stable over wide range of pH 2 - 12 | |
Nanosphere | |
95 | |
LG | |
N[C@@H](CC(C)C)C(=O)NCC=O | |